dbPTM

NIT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NIT2_HUMAN
UniProt AC	Q9NQR4
Protein Name	Omega-amidase NIT2
Gene Name	NIT2
Organism	Homo sapiens (Human).
Sequence Length	276
Subcellular Localization	Cytoplasm .
Protein Description	Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting alpha-ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively. Overexpression decreases the colony-forming capacity of cultured cells by arresting cells in the G2 phase of the cell cycle..
Protein Sequence	MTSFRLALIQLQISSIKSDNVTRACSFIREAATQGAKIVSLPECFNSPYGAKYFPEYAEKIPGESTQKLSEVAKECSIYLIGGSIPEEDAGKLYNTCAVFGPDGTLLAKYRKIHLFDIDVPGKITFQESKTLSPGDSFSTFDTPYCRVGLGICYDMRFAELAQIYAQRGCQLLVYPGAFNLTTGPAHWELLQRSRAVDNQVYVATASPARDDKASYVAWGHSTVVNPWGEVLAKAGTEEAIVYSDIDLKKLAEIRQQIPVFRQKRSDLYAVEMKKP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
26	Phosphorylation	DNVTRACSFIREAAT CCHHHHHHHHHHHHH	23.79	25159151
37	Acetylation	EAATQGAKIVSLPEC HHHHCCCEEEECHHH	50.92	26051181
37	Ubiquitination	EAATQGAKIVSLPEC HHHHCCCEEEECHHH	50.92	-
47	Phosphorylation	SLPECFNSPYGAKYF ECHHHHCCCCCHHCC	10.15	28152594
49	Phosphorylation	PECFNSPYGAKYFPE HHHHCCCCCHHCCHH	29.54	20090780
52	Ubiquitination	FNSPYGAKYFPEYAE HCCCCCHHCCHHHHH	42.96	-
52	Acetylation	FNSPYGAKYFPEYAE HCCCCCHHCCHHHHH	42.96	25953088
60	Ubiquitination	YFPEYAEKIPGESTQ CCHHHHHHCCCCCHH	46.13	-
65	Phosphorylation	AEKIPGESTQKLSEV HHHCCCCCHHHHHHH	41.89	20068231
68	Acetylation	IPGESTQKLSEVAKE CCCCCHHHHHHHHHH	54.81	25953088
68	Succinylation	IPGESTQKLSEVAKE CCCCCHHHHHHHHHH	54.81	-
68	Succinylation	IPGESTQKLSEVAKE CCCCCHHHHHHHHHH	54.81	-
68	Ubiquitination	IPGESTQKLSEVAKE CCCCCHHHHHHHHHH	54.81	-
92	Ubiquitination	IPEEDAGKLYNTCAV CCHHHHCHHCEECEE	49.90	-
96	Phosphorylation	DAGKLYNTCAVFGPD HHCHHCEECEEECCC	6.57	22210691
109	Ubiquitination	PDGTLLAKYRKIHLF CCCCEEEEEEEEEEE	45.62	-
112	Ubiquitination	TLLAKYRKIHLFDID CEEEEEEEEEEEECC	31.24	-
123	Acetylation	FDIDVPGKITFQESK EECCCCCEEEEEECC	32.29	25953088
123	Succinylation	FDIDVPGKITFQESK EECCCCCEEEEEECC	32.29	-
123	Succinylation	FDIDVPGKITFQESK EECCCCCEEEEEECC	32.29	-
125	Phosphorylation	IDVPGKITFQESKTL CCCCCEEEEEECCCC	23.81	28857561
129	Phosphorylation	GKITFQESKTLSPGD CEEEEEECCCCCCCC	21.84	28857561
130	Ubiquitination	KITFQESKTLSPGDS EEEEEECCCCCCCCC	53.37	-
130	Succinylation	KITFQESKTLSPGDS EEEEEECCCCCCCCC	53.37	-
130	Succinylation	KITFQESKTLSPGDS EEEEEECCCCCCCCC	53.37	-
131	Phosphorylation	ITFQESKTLSPGDSF EEEEECCCCCCCCCC	41.57	28857561
133	Phosphorylation	FQESKTLSPGDSFST EEECCCCCCCCCCCC	31.88	21815630
137	Phosphorylation	KTLSPGDSFSTFDTP CCCCCCCCCCCCCCC	27.32	28857561
139	Phosphorylation	LSPGDSFSTFDTPYC CCCCCCCCCCCCCCH	31.92	28152594
140	Phosphorylation	SPGDSFSTFDTPYCR CCCCCCCCCCCCCHH	24.42	28152594
143	Phosphorylation	DSFSTFDTPYCRVGL CCCCCCCCCCHHCCC	16.38	28152594
145	Phosphorylation	FSTFDTPYCRVGLGI CCCCCCCCHHCCCCE	8.59	20090780
165	Phosphorylation	FAELAQIYAQRGCQL HHHHHHHHHHCCCEE	5.65	28152594
202	Phosphorylation	RAVDNQVYVATASPA CCCCCEEEEEECCCC	3.74	27642862
207	Phosphorylation	QVYVATASPARDDKA EEEEEECCCCCCCCC	18.10	-
237	Phosphorylation	EVLAKAGTEEAIVYS HHHHHCCCCEEEEEE	35.20	18452278
244	Phosphorylation	TEEAIVYSDIDLKKL CCEEEEEECCCHHHH	19.73	-
249	Ubiquitination	VYSDIDLKKLAEIRQ EEECCCHHHHHHHHH	41.83	-
249	Acetylation	VYSDIDLKKLAEIRQ EEECCCHHHHHHHHH	41.83	25953088
250	Acetylation	YSDIDLKKLAEIRQQ EECCCHHHHHHHHHH	61.29	2380219
250	Ubiquitination	YSDIDLKKLAEIRQQ EECCCHHHHHHHHHH	61.29	-
265	Dimethylation	IPVFRQKRSDLYAVE CHHHHHCCCCEEEEE	27.37	-
265	Methylation	IPVFRQKRSDLYAVE CHHHHHCCCCEEEEE	27.37	24377505
266	Phosphorylation	PVFRQKRSDLYAVEM HHHHHCCCCEEEEEE	38.72	25159151
269	Phosphorylation	RQKRSDLYAVEMKKP HHCCCCEEEEEECCC	17.37	19060867

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of NIT2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NIT2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of NIT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NPTX1_HUMAN	NPTX1	physical	22939629
PRDX6_HUMAN	PRDX6	physical	22939629
SUCB1_HUMAN	SUCLA2	physical	22939629
TIM9_HUMAN	TIMM9	physical	22939629
TOIP1_HUMAN	TOR1AIP1	physical	22939629
TMEDA_HUMAN	TMED10	physical	22939629
OPA1_HUMAN	OPA1	physical	22939629
RM12_HUMAN	MRPL12	physical	22939629
PPT1_HUMAN	PPT1	physical	22939629
RNT2_HUMAN	RNASET2	physical	22939629
NPTN_HUMAN	NPTN	physical	22939629
PGM1_HUMAN	PGM1	physical	22939629
TM177_HUMAN	TMEM177	physical	22939629
TM189_HUMAN	TMEM189	physical	22939629
LDHA_HUMAN	LDHA	physical	26344197
PARK7_HUMAN	PARK7	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
PSMG4_HUMAN	PSMG4	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NIT2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266 AND TYR-269, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND MASSSPECTROMETRY.	15592455 [Abstract]